Abstract
The study of that group of diseases now collectively known as the prion diseases has always been a source of excitement and argument between scientists. These obscure diseases usually have been of extremely rare occurrence and have had little impact on the general public. When an epidemic occurs, however, as in the case of bovine spongiform encephalopathy (BSE) in the United Kingdom, the bizarreness of the prion diseases and the profound difference between them and any other “infectious” condition can (and did) lead to public consternation. Three features of prion diseases give them an apparently diabolical quality.
This is a preview of subscription content, log in via an institution to check access.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
References
Hsiao, K K, Groth, D, Scott, M, Yang, S.-L., Serban, H., Rapp, D, Foster, D, et al (1994) Serial transmission in rodents of neurodegeneratron from transgenic mice expressing mutant prion protein. Proc Natl Acad Sci USA 91, 9126–9130.
Kocisko, D A, Come, J H., Priola, S. A, Chesebro, B, Raymond, G J, Lansbury, P T, et al. (1994) Cell-free formation of protease-resistant prion protein. Nature 370, 471–474.
Glasse, R and Lindenbaum, S (1992) Fieldwork in the South Fore: the process of ethnographic inquiry, in Prion Diseases of Humans and Animals (Prusiner, S. B., Collinge, J., Powell, J., and Anderton, B., eds.), Ellis Horwood, London, pp 77–91
Hsiao, K, Baker, H F, Crow, T J, Poulter, M, Owen, F, Terwilliger, J D, et al. (1989) Linkage of a prion protein missense variant to Gerstmann-Straussler syndrome. Nature 338, 342–345
Poulter, M., Baker, H. F., Frith, C D, Leach, M., Lofthouse, R., Ridley, R M., et al (1992) Inherited prion disease with 144 base pair gene insertion 1 Genealogical and molecular studies. Brain 115, 675–685
Palmer, M S, Dryden, A J, Hughes, J T, and Collinge, J (1991) Homozygous prion protein genotype predisposes to sporadic Creutzfeldt-Jakob disease. Nature 352, 340–342.
Parry, H B. (1983) Scrapie Disease in Sheep. Historical, Clinical, Epidemiological and Practical Aspects of the Natural Disease, Academic, London.
Goldman, W., Hunter, N., Foster, J. D., Salbaum, J. M., Beyreuther, K, and Hope, J (1990) Two alleles of a neural protein gene linked to scrapie in sheep. Proc Natl Acad Sci USA 87, 2476–2480.
Westaway, D, DeArmond, S. J, Cayetanocanlas, J, Groth, D., Foster, D., Yang, S. L, et al (1994) Degeneration of skeletal muscle, pertpheral nerves, and the central nervous system in transgenic mice overexpressing wild-type prion proteins. Cell 76, 117–129.
Pattison, I H (1974) Scrapie in sheep selectively bred for high susceptibility. Nature 248, 594–595
Dickinson, A. G, Stamp, J T., and Renwick, C. C (1974) Maternal and lateral transmission of scrapie in sheep. J Comp Pathol 84, 19–25
Pattison, I H, Hoare, M. N., Jebbett, J N., and Watson, W. A. (1972) Spread of scrapie to sheep and goats by oral dosing with foetal membranes from scrapieaffected sheep. Vet. Rec. 90, 465–468
Foster, J D., McKelvey, W. A. C., Mylne, M J. A, Williams, A, Hunter, N, Hope, J, et al (1992) Studies on maternal transmission of scraple in sheep by embryo transfer. Vet Rec 130, 341–343.
Pattison, I. H. (1992) A sideways look at the scrapie saga, in Prion Diseases of Humans and Animals (Prusiner, S. B, Collinge, J, Powell, J, and Anderton, B, eds), Ellis Horwood, London, pp. 16–22.
Caspar, D. L. D. (1991) Self-control of self-assembly. Nature 315 331–333
Cheng, M. Y, Hartl, F-U, and Horwich, A L (1990) The mitochondrial chaperonin hsp60 is required for its own assembly. Nature 348, 455–458
Milner, J. and Medcalf, E. A. (1991) Cotranslation of activated mutant p53 with wild type drives the wild type p53 protein into the mutant conformation. Cell 65, 766–774.
Huang, Z., Gabriel, J.-M, Baldwin, M A., Fletterick, R J, Prusiner, S B, and Cohen, F E (1994) Proposed three-dimensional structure for the cellular prion protein. Proc Natl Acad Sci USA 91, 7139–7143.
Jeffrey, M, Goodsir, C M, Bruce, M, McBride, P A, Scott, J. R, and Halliday, W G. (1994) Correlative light and electron microscopy studies of PrP localisation in 87V scrapie. Brain Res 656, 329–343.
Tagliavini, F, Prelli, F, Ghiso, J, Bugiani, 0, Serban, D, Prusmer, S B, et al. (1991) Amyloid protein of Gerstmann-Straussler-Scheinker disease (Indiana kindred) is an 11 kd fragment of prion protein with an N-terminal glycine at codon 58. EMBO J 10, 513–519
Pearson, R C A., Esiri, M M., Hiorns, R. W, Wilcock, G K., and Powell, T P S (1985) Anatomical correlates of the distribution of the pathological changes in the neocortex in Alzhelmer disease. Proc Natl. Acad Sci USA 82, 4531–4534
Baker, H. F, Ridley, R. M, Duchen, L W., Crow, T. J., and Bruton, C J. (1994) Induction of P-amyloid in primates by injection of Alzheimer’s disease brain homogenate: comparison with transmission of spongiform encephalopathy. Mol Neurobiol 8, 25–40
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 1996 Humana Press Inc., Totowa, NJ
About this protocol
Cite this protocol
Ridley, R.M., Baker, H.F. (1996). The Paradox of Prion Disease. In: Baker, H.F., Ridley, R.M. (eds) Prion Diseases. Methods in Molecular Medicine, vol 3. Springer, Totowa, NJ. https://doi.org/10.1385/0-89603-342-2:1
Download citation
DOI: https://doi.org/10.1385/0-89603-342-2:1
Publisher Name: Springer, Totowa, NJ
Print ISBN: 978-0-89603-342-9
Online ISBN: 978-1-59259-587-7
eBook Packages: Springer Protocols